catalytic activity:Preferentially cleaves the C-terminal side of arginine residues at the P1 position of certain peptides, cleaving Boc-Phe-Ser-Arg-4-methylcoumaryl-7-amide most efficiently and having an optimum pH of 8.6 with this substrate.,enzyme regulation:Strongly inhibited by diisopropyl fluorophosphate, leupeptin, antipain, aprotinin, and soybean trypsin inhibitor, but hardly inhibited by secretory leukocyte protease inhibitor at 10 microM.,function:May play some biological role in the host defense system on the mucous membrane independently of or in cooperation with other substances in airway mucous or bronchial secretions.,similarity:Belongs to the peptidase S1 family.,similarity:Contains 1 peptidase S1 domain.,similarity:Contains 1 SEA domain.,subcellular location:Activated by cleavage and secreted.,subunit:Monomer.,tissue specificity:Located in the cells of the submucosal serous glands of the bronchi and trachea.,
Cell membrane; Single-pass type II membrane protein. Activated by cleavage and secreted.; [Transmembrane protease serine 11D catalytic chain]: Secreted. Activated by cleavage and secreted.
Located in the cells of the submucosal serous glands of the bronchi and trachea.
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